TP1A_RANDY
ID TP1A_RANDY Reviewed; 14 AA.
AC P0C5X6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 17-JUN-2020, entry version 14.
DE RecName: Full=Temporin-1DYa;
OS Rana dybowskii (Dybovsky's frog) (Korean brown frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=71582;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT GLY-14, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=17688900; DOI=10.1016/j.toxicon.2007.06.023;
RA Conlon J.M., Kolodziejek J., Nowotny N., Leprince J., Vaudry H., Coquet L.,
RA Jouenne T., Iwamuro S.;
RT "Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families
RT isolated from the skin of the Japanese brown frog, Rana dybowskii.";
RL Toxicon 50:746-756(2007).
CC -!- FUNCTION: Antimicrobial peptide. Active against the Gram-positive
CC bacterium S.aureus (MIC>60 uM) and the Gram-negative bacterium E.coli
CC (MIC>60 uM). {ECO:0000269|PubMed:17688900}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: Mass=1403.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17688900};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..14
FT /note="Temporin-1DYa"
FT /id="PRO_0000311604"
FT MOD_RES 14
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:17688900"
SQ SEQUENCE 14 AA; 1406 MW; 9D0EAF727CACF3C5 CRC64;
FIGPIISALA SLFG